Search results for "Poly(acrylamide)"

showing 10 items of 377 documents

Killer toxin of Hanseniaspora uvarum

1990

The yeast Hanseniaspora uvarum liberates a killer toxin lethal to sensitive strains of the species Saccharomyces cerevisiae. Secretion of this killer toxin was inhibited by tunicamycin, an inhibitor of N-glycosylation, although the mature killer protein did not show any detectable carbohydrate structures. Culture supernatants of the killer strain were concentrated by ultrafiltration and the extracellular killer toxin was precipitated with ethanol and purified by ion exchange chromatography. SDS-PAGE of the electrophoretically homogenous killer protein indicated an apparent molecular mass of 18,000. Additional investigations of the primary toxin binding sites within the cell wall of sensitiv…

GlycosylationSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaechemical and pharmacologic phenomenaSaccharomyces cerevisiaemedicine.disease_causeHanseniasporaBiochemistryMicrobiologyMicrobiologyFungal Proteinschemistry.chemical_compoundCell WallGeneticsmedicineExtracellularSecretionIsoelectric PointGlucansMolecular BiologyBinding SitesbiologyMolecular massToxinGeneral MedicineTunicamycinMycotoxinsChromatography Ion Exchangebiology.organism_classificationKiller Factors YeastYeastBiochemistrychemistrySaccharomycetalesElectrophoresis Polyacrylamide GelArchives of Microbiology
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Cell wall mannoproteins during the population growth phases in Saccharomyces cerevisiae.

1987

Mannoproteins from cell walls of Saccharomyces cerevisiae synthesized at successive stages of the population growth cycle have been solubilized with Zymolyase and subsequently analyzed. The major change along the population cycle concerned a large size mannoprotein material; the size of the newly-synthesized molecules varied from 120,000–500,000 (mean of about 200,000) at early exponential phase to 250,000–350,000 (mean of about 300,000) at late exponential phase. These differences are due to modifications in the amount of N-glycosidically linked mannose residues, since the size of the peptide moiety was 90,000–100,000 at all growth stages and the level of O-glycosylation changed only sligh…

GlycosylationSaccharomyces cerevisiaeMannosePeptideSaccharomyces cerevisiaeBiologyBiochemistryMicrobiologylaw.inventionCell wallFungal Proteinschemistry.chemical_compoundlawCell WallGeneticsConcanavalin AMolecular BiologyIncubationGlucanGlycoproteinschemistry.chemical_classificationMembrane GlycoproteinsGlucan Endo-13-beta-D-GlucosidaseSodium Dodecyl SulfateGeneral Medicinebiology.organism_classificationcarbohydrates (lipids)Molecular WeightDithiothreitolMicroscopy ElectronchemistryBiochemistryConcanavalin AFerritinsbiology.proteinChromatography GelElectrophoresis Polyacrylamide GelElectron microscopeArchives of microbiology
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Isolation of carcinoembryonic antigen N-terminal domains (N-A1) from soluble aggregates

2011

Abstract Carcinoembryonic antigen (CEA) was identified as a prominent tumor-associated antigen in human colorectal cancer and it is still intensively investigated. However, its physiological role remains unclear. The CEA molecule is composed of seven highly hydrophobic, immunoglobulin-like domains, six of which contain a single disulphide bridge. The production of recombinant protein containing Ig-like domains in bacterial expression systems often results in partial degradation or insolubility due to aggregation hampering the analysis of their native structure and function. Here, we present a new method of expression and purification of CEA N-terminal domains (N-A1) fused to MBP in Escheric…

Guanidinium chlorideCircular dichroismRecombinant Fusion Proteinsmedicine.disease_causeMaltose-Binding Proteinslaw.inventionchemistry.chemical_compoundCarcinoembryonic antigenlawProtein purificationEscherichia colimedicineTEV proteaseHumansDisulfidesEscherichia coliGuanidinebiologyProtein StabilityCircular DichroismFusion proteinCarcinoembryonic AntigenProtein Structure TertiarySolubilitychemistryBiochemistryChromatography GelRecombinant DNAbiology.proteinElectrophoresis Polyacrylamide GelBiotechnologyProtein Expression and Purification
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Carbohydrate binding specificity and purification by biospecific affinity chromatography of Ascidiamalaca traust. Hemagglutinins

1982

The carbohydrate specificities of Ascidia malaca serum hemagglutinins were determined by hemagglutination inhibition tests. Analysis of agglutinins against rabbit and human A, B, O erythrocytes suggests that the size of the combining site corresponds to a disaccharide with a specificity for saccharides containing a D-galacto configuration (D-melibiose, D-raffinose, D-galactose, alpha-lactose, lactulose, L-arabinose). No anomeric specificity was observed with oligosaccharides. Hydroxyl groups probably involved in hydrogen-bond formation with agglutinin binding site, were identified as carbons C2, C4, C5 and C6 of D-galactose. Absorption experiments showed that two distinct agglutinins with s…

Hemagglutination Inhibition TestsErythrocytesImmunologyDisaccharideBiologyChromatography Affinitychemistry.chemical_compoundRaffinoseAgglutininSpecies SpecificityAffinity chromatographyAnimalsHumansUrochordataBinding sitePolyacrylamide gel electrophoresisBinding selectivityMelibioseBinding SitesGalactoseHemagglutination TestsHemagglutination Inhibition TestsAgglutination (biology)HemagglutininschemistryBiochemistryAntibody FormationCarbohydrate MetabolismRabbitsDevelopmental BiologyDevelopmental & Comparative Immunology
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Evolution of tissue-specific keratins as deduced from novel cDNA sequences of the lungfish Protopterus aethiopicus.

2005

Lungfishes are possibly the closest extant relatives of the land vertebrates (tetrapods). We report here the cDNA and predicted amino acid sequences of 13 different keratins (ten type I and three type II) of the lungfish Protopterus aethiopicus. These keratins include the orthologs of human K8 and K18. The lungfish keratins were also identified in tissue extracts using two-dimensional polyacrylamide gel electrophoresis, keratin blot binding assays and immunoblotting. The identified keratin spots were analyzed by peptide mass fingerprinting which assigned seven sequences (inclusively Protopterus K8 and K18) to their respective protein spot. The peptide mass fingerprints also revealed the fac…

HistologyDNA ComplementaryMolecular Sequence DataFluorescent Antibody Techniquemacromolecular substancesPeptide MappingPathology and Forensic MedicineEvolution MolecularPeptide mass fingerprintingComplementary DNAKeratinAnimalsElectrophoresis Gel Two-DimensionalAmino Acid SequencePolyacrylamide gel electrophoresisLungfishchemistry.chemical_classificationProtopterusintegumentary systembiologyPhylogenetic treeLampreyFishesCell BiologyGeneral MedicineAnatomybiology.organism_classificationchemistryEvolutionary biologySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationKeratinsEuropean journal of cell biology
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Tracing keratin evolution: catalog, expression patterns and primary structure of shark (Scyliorhinus stellaris) keratins.

1998

We have studied individual keratins of an elasmobranch, the shark Scyliorhinus stellaris (the lesser-spotted dogfish). From various shark tissues, notably skin and stomach, cytoskeletal proteins were isolated and then separated by two-dimensional polyacrylamide gel electrophoresis. Using complementary keratin blot-binding assays and immunoblotting, among these proteins we identified a variety of type I and type II keratins. According to their tissue-specific expression, we distinguished Is and IIs keratins from IE and IIE keratins ("S" and "E" from "simple epithelial" and "epidermal", respectively). Guinea pig antibodies which in immunoblots specifically labeled the entire range of identifi…

HistologyDNA ComplementaryMolecular Sequence Datamacromolecular substancesPathology and Forensic MedicineKeratinAnimalsHumansAmino Acid SequenceIntermediate filamentPolyacrylamide gel electrophoresisPeptide sequencechemistry.chemical_classificationintegumentary systemPhylogenetic treebiologyBase SequenceProtein primary structureCell BiologyGeneral MedicineKeratin 6Abiology.organism_classificationMolecular biologyBiological EvolutionchemistryMicroscopy FluorescenceSharksKeratinshuman activitiesScyliorhinus stellarisEuropean journal of cell biology
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Sequence, evolution and tissue expression patterns of an epidermal type I keratin from the shark Scyliorhinus stellaris.

2004

From the shark Scyliorhinus stellaris we cloned and sequenced a cDNA encoding a novel type I keratin, termed SstK10. By MALDI-MS peptide mass fingerprinting of cytoskeletal proteins separated on polyacrylamide gels, we assigned SstK10 to a 46-kDa protein which is the major epidermal type I (“IE”) keratin in this fish and is specifically expressed in stratified epithelia. In a phylogenetic tree based on type I keratin sequences and with lamprey keratins applied as outgroup, SstK10 branches off in a rather basal position. This tree strongly supports the concept that teleost keratins and tetrapod keratins resulted from two independent gene radiation processes. The only exception is human K18 b…

HistologyDNA ComplementaryType I keratinMolecular Sequence Datamacromolecular substancesMass SpectrometryPathology and Forensic MedicineSequence Analysis Proteinbiology.animalKeratinAnimalsAmino Acid SequenceCloning MolecularPhylogenychemistry.chemical_classificationintegumentary systemPhylogenetic treebiologyLampreyVertebrateCell BiologyGeneral MedicineGnathostomataKeratin 6AAnatomybiology.organism_classificationImmunohistochemistryCell biologychemistryEpidermal CellsGene Expression RegulationOrgan SpecificitySharksKeratinsElectrophoresis Polyacrylamide GelEpidermisScyliorhinus stellarisEuropean journal of cell biology
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Candida albicans mycelial wall structure: supramolecular complexes released by zymolyase, chitinase and beta-mercaptoethanol.

1991

Different techniques released from the wall of Candida albicans mycelial cells high molecular weight mannoprotein materials with different levels of complexity. SDS solubilized among others one protein of 180 kDa which reacted with a monoclonal antibody (MAb) specific of a O-glycosylated protein secreted by regenerating mycelial protoplasts [Elorza et al. (1989) Biochem Biophys Res Commun 162:1118-1125]. Zymolyase, chitinase and beta-mercaptoethanol, released different types of high molecular highly polydisperse mannoprotein materials (greater than 180 kDa) that also reacted with the same MAb. These materials had N-glycosidically linked sugar chains, in addition to the O-glycosidically bond…

HydrolasesBlotting WesternMannoseGerm tubeChitinBiologyBiochemistryMicrobiologyCell wallchemistry.chemical_compoundChitinCell WallCandida albicansGeneticsSodium dodecyl sulfateCandida albicansMolecular BiologyPolyacrylamide gel electrophoresisMembrane GlycoproteinsHydrolysisChitinasesSodium Dodecyl SulfateGeneral Medicinebiology.organism_classificationcarbohydrates (lipids)Microscopy ElectronHexosaminidasesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidasechemistryBiochemistrySolubilityChitinasebiology.proteinChromatography GelElectrophoresis Polyacrylamide GelArchives of microbiology
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Sponge aggregation factor and sponge hemagglutinin: possible relationships between two different molecules.

1979

Abstract A lectin from the marine sponge GEODIA CYDONIUM was isolated and characterized. GEODIA lectin (GL) agglutinates human red blood cells irrespective of the ABO blood group and precipitates with a variety of D -galactose containing glycosubstances, i.e. certain snail galactans, bovine erythrocyte glycoprotein and PNEUMOCOCCUS type XIV polysaccharide. The only simple sugars inhibiting the GL-mediated hemagglutination were lactose and n -acetyl- D -galactosamine. GL was purified by affinity chromatography on Sepharose 4B almost to homogeneity as tested by polyacrylamide disc gel electrophoresis. Positive staining of the lectin band with Coomassie brilliant blue and PAS suggest that GL i…

ImmunodiffusionHot TemperatureImmunologyOligosaccharidesBiologySepharosechemistry.chemical_compoundAffinity chromatographyLectinsAnimalsGeodiaCell AggregationCoomassie Brilliant BlueLectinHemagglutininHemagglutination Inhibition Testsbiology.organism_classificationCell aggregationPoriferaMolecular WeightHemagglutininschemistryBiochemistryAgglutininsGalactosebiology.proteinChromatography GelElectrophoresis Polyacrylamide GelDevelopmental BiologyDevelopmental and comparative immunology
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Recombinant virus-like particles as a carrier of B- and T-cell epitopes of hepatitis C virus (HCV)

2005

The major aim of the project was the development of virus-like particles (VLP) displaying B- and T-cell epitopes of hepatitis C virus (HCV) proteins. To this end, hepatitis B virus core (HBc) particles were used as a carrier of HCV epitopes. Fragments of HCV genes encoding core (aa 98) and NS3 (aa 155) proteins were fused to the 3' terminus of the truncated HBV core gene. All recombinant plasmids led to relatively high levels of expression of chimeric proteins in E. coli, which resulted in the formation of complete "mature" VLP. Chimeric HBc/HCV VLPs were purified by combination of gel filtration and sucrose gradient centrifugation, and used for immunogenicity studies in mice. All variants …

ImmunogenT-LymphocytesvirusesHepacivirusBiologyRecombinant virusEpitopeVirusEpitopesMiceVirus-like particleAnimalsCell ProliferationB-LymphocytesMice Inbred BALB CNS3General VeterinaryGeneral Immunology and MicrobiologyImmunogenicityVirionPublic Health Environmental and Occupational Healthvirus diseasesVirologyMolecular biologydigestive system diseasesHBcAgInfectious DiseasesMolecular MedicineElectrophoresis Polyacrylamide GelFemaleVaccine
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